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Conserved domains on  [gi|1510996204|gb|AYU58846|]
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neomycin phosphotransferase [Cloning vector pEASY-tub/hptII]

Protein Classification

aminoglycoside 3'-phosphotransferase( domain architecture ID 10790026)

aminoglycoside 3'-phosphotransferase phosphorylates and inactives antibiotic substrates such as kanamycin, streptomycin, neomycin, and gentamicin, among others

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
8-264 1.35e-124

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 354.61  E-value: 1.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204   8 HAGSPAAWVERLFGYDWAQQTIGCSDAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGVPCAAVLDVVTEA 87
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQGLPVPEVLDFGEDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  88 GRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGL 165
Cdd:COG3231    81 GGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEERRGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 166 APAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYG 245
Cdd:COG3231   161 PPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEGWVEPFLDAYG 240

                         250
                  ....*....|....*....
gi 1510996204 246 IaAPDSQRIAFYRLLDEFF 264
Cdd:COG3231   241 I-APDPERLAFYRLLDEFF 258
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
8-264 1.35e-124

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 354.61  E-value: 1.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204   8 HAGSPAAWVERLFGYDWAQQTIGCSDAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGVPCAAVLDVVTEA 87
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQGLPVPEVLDFGEDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  88 GRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGL 165
Cdd:COG3231    81 GGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEERRGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 166 APAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYG 245
Cdd:COG3231   161 PPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEGWVEPFLDAYG 240

                         250
                  ....*....|....*....
gi 1510996204 246 IaAPDSQRIAFYRLLDEFF 264
Cdd:COG3231   241 I-APDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 22-264 1.23e-111

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 321.45  E-value: 1.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  22 YDWAQQTIGCSDAAVFRLSAqGRPVLFVKTDLSGALNELQDEAARLSWLATTgVPCAAVLDVVTEAGRDWLLLGEVPGQD 101
Cdd:cd05150     1 YRWEPDTIGESGARVYRLDG-GGPVLYLKTAPAGYAYELAREAERLRWLAGK-LPVPEVLDYGSDDGGDWLLTTALPGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 102 LLSSH--LAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGLAPAELFARLKARMP 179
Cdd:cd05150    79 AASLEplLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEATRP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 180 DGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGE-WADRFLVLYGIAAPDSQRIAFYR 258
Cdd:cd05150   159 AEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEeYAERFLDAYGIDAPDPERLAYYR 238


                  ....*.
gi 1510996204 259 LLDEFF 264
Cdd:cd05150   239 LLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 33-251 1.94e-30

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 113.75  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  33 DAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGV-PCAAVLDVVTEA---GRDWLLLGEVPGQDLLSSHLA 108
Cdd:pfam01636  10 SNRTYLVTTGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVpPVPRVLAGCTDAellGLPFLLMEYLPGEVLARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 109 PAEKVSI--MADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGLAPAELFARLKARMPDGEDLVV 186
Cdd:pfam01636  90 EERGALLeaLGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALLALLPAELPPVL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510996204 187 THGDACLPNIMV-ENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYGIAAPDS 251
Cdd:pfam01636 170 VHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYAR 235
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
8-264 1.35e-124

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 354.61  E-value: 1.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204   8 HAGSPAAWVERLFGYDWAQQTIGCSDAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGVPCAAVLDVVTEA 87
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQGLPVPEVLDFGEDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  88 GRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGL 165
Cdd:COG3231    81 GGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEERRGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 166 APAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYG 245
Cdd:COG3231   161 PPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEGWVEPFLDAYG 240

                         250
                  ....*....|....*....
gi 1510996204 246 IaAPDSQRIAFYRLLDEFF 264
Cdd:COG3231   241 I-APDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 22-264 1.23e-111

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 321.45  E-value: 1.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  22 YDWAQQTIGCSDAAVFRLSAqGRPVLFVKTDLSGALNELQDEAARLSWLATTgVPCAAVLDVVTEAGRDWLLLGEVPGQD 101
Cdd:cd05150     1 YRWEPDTIGESGARVYRLDG-GGPVLYLKTAPAGYAYELAREAERLRWLAGK-LPVPEVLDYGSDDGGDWLLTTALPGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 102 LLSSH--LAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGLAPAELFARLKARMP 179
Cdd:cd05150    79 AASLEplLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEATRP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 180 DGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGE-WADRFLVLYGIAAPDSQRIAFYR 258
Cdd:cd05150   159 AEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEeYAERFLDAYGIDAPDPERLAYYR 238


                  ....*.
gi 1510996204 259 LLDEFF 264
Cdd:cd05150   239 LLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 33-251 1.94e-30

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 113.75  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  33 DAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGV-PCAAVLDVVTEA---GRDWLLLGEVPGQDLLSSHLA 108
Cdd:pfam01636  10 SNRTYLVTTGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVpPVPRVLAGCTDAellGLPFLLMEYLPGEVLARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 109 PAEKVSI--MADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGLAPAELFARLKARMPDGEDLVV 186
Cdd:pfam01636  90 EERGALLeaLGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALLALLPAELPPVL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510996204 187 THGDACLPNIMV-ENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYGIAAPDS 251
Cdd:pfam01636 170 VHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYAR 235
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 33-264 1.39e-19

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 85.55  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  33 DAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLA-TTGVPCAAVLDVVTEA---GRDWLLLGEVPGQDLLS--SH 106
Cdd:COG3173    33 SNLTYRLDTGDRLVLRRPPRGLASAHDVRREARVLRALApRLGVPVPRPLALGEDGeviGAPFYVMEWVEGETLEDalPD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 107 LAPAEKVSI---MADAMRRLHTLDPATCPFD----HQAKHRIERARTRMEAGLVDQDDLDEehqglAPAELFARLKARMP 179
Cdd:COG3173   113 LSPAERRALaraLGEFLAALHAVDPAAAGLAdgrpEGLERQLARWRAQLRRALARTDDLPA-----LRERLAAWLAANLP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 180 DGEDLVVTHGDACLPNIMV--ENGRFSGFIDCGRLGVADRYQDIA--LATRDIAEELGGEwADRFLVLYGIAAPDSQRIA 255
Cdd:COG3173   188 EWGPPVLVHGDLRPGNLLVdpDDGRLTAVIDWELATLGDPAADLAylLLYWRLPDDLLGP-RAAFLAAYEEATGDLDDLT 266


                  ....*....
gi 1510996204 256 FYRLLDEFF 264
Cdd:COG3173   267 WWALADPEL 275
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 63-250 1.14e-11

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 63.02  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  63 EAARLSWLATTGVPCAAVLDVVTEA---GRDWLLL----GEVPGQDLLSSHLAPAEKVSI---MADAMRRLHTLDPATCP 132
Cdd:cd05154    48 EYRVLRALAGTGVPVPRVLALCEDPsvlGAPFYVMervdGRVLPDPLPRPDLSPEERRALarsLVDALAALHSVDPAALG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 133 FDHQAKHR------IERARTRMEAGLVDQDDLDEEhqglapaeLFARLKARMPDGEDLVVTHGDACLPNIMV-ENGRFSG 205
Cdd:cd05154   128 LADLGRPEgylerqVDRWRRQLEAAATDPPPALEE--------ALRWLRANLPADGRPVLVHGDFRLGNLLFdPDGRVTA 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1510996204 206 FIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYGIAAPD 250
Cdd:cd05154   200 VLDWELATLGDPLEDLAWLLARWWRPGDPPGLAAPTRLPGFPSRE 244
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 33-230 7.97e-10

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 56.16  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  33 DAAVFRLSAQGRPVLFVKTDLsgALNELQDEAARLSWLA-TTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSH--LAP 109
Cdd:cd05120    11 DNKVYLLGDPREYVLKIGPPR--LKKDLEKEAAMLQLLAgKLSLPVPKVYGFGESDGWEYLLMERIEGETLSEVWprLSE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 110 AEKVSIM---ADAMRRLHTLDPatcpfdhqakhrierartrmeaglvdqddldeehqglapaelfarlkarmpdgedLVV 186
Cdd:cd05120    89 EEKEKIAdqlAEILAALHRIDS-------------------------------------------------------SVL 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1510996204 187 THGDACLPNIMVEN-GRFSGFIDCGRLGVADRYQDIALATRDIAE 230
Cdd:cd05120   114 THGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 59-230 1.34e-08

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 54.55  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  59 ELQDEAARLSWLATTGVPCAAVL------DVVTEAGRDWLLLGEVPGQDLLSSHLAPAEkvsIMADAMRRLHTldpATCP 132
Cdd:COG2334    53 EIPFELALLAHLAAAGLPVPAPVptrdgeTLLELEGRPAALFPFLPGRSPEEPSPEQLE---ELGRLLARLHR---ALAD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 133 FDHQAKHRIErARTRMEAGLVDQDDLDEEHQGLAPAEL--FARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDCG 210
Cdd:COG2334   127 FPRPNARDLA-WWDELLERLLGPLLPDPEDRALLEELLdrLEARLAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFD 205

                         170       180
                  ....*....|....*....|
gi 1510996204 211 RLGVADRYQDIALATRDIAE 230
Cdd:COG2334   206 DAGYGPRLYDLAIALNGWAD 225
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 59-224 7.07e-07

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 49.18  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  59 ELQDEAARLSWLATTGVPCAAVL------DVVTEAGRDWLLLGEVPGQDLLSSHlapAEKVSIMADAMRRLHTldpATCP 132
Cdd:cd05153    53 ELPFELELLDHLAQAGLPVPRPLadkdgeLLGELNGKPAALFPFLPGESLTTPT---PEQCRAIGAALARLHL---ALAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 133 FDHQAKHR---------IERARTRmeAGLVDQDDLDEEhqglapAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRF 203
Cdd:cd05153   127 FPPPRPNPrglawwkplAERLKAR--LDLLAADDRALL------EDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRL 198

                         170       180
                  ....*....|....*....|.
gi 1510996204 204 SGFIDCGRLGVADRYQDIALA 224
Cdd:cd05153   199 SGIIDFYDACYDPLLYDLAIA 219
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 117-216 8.15e-05

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 42.61  E-value: 8.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 117 ADAMRRLHTLDPATCPFDHQAKH---RIERARTRMEAGLVDQDDLDEEhqglAPAELFARLKARMPDGEDLVVTHGDACL 193
Cdd:cd05155    97 ARFLAALHAIDPAGPPNPGRGNPlrgRDLAVRDAEEALAALAGLLDVA----AARALWERALAAPAWAGPPVWLHGDLHP 172

                          90       100
                  ....*....|....*....|...
gi 1510996204 194 PNIMVENGRFSGFIDCGRLGVAD 216
Cdd:cd05155   173 GNLLVRDGRLSAVIDFGDLGVGD 195
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
122-263 1.37e-04

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 41.31  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204 122 RLHTLdPATCPFDhqAKHRIERARtrmeaglvdqDDLDEEHQGLApaELFARLKARMP-DGEDLVVTHGDACLPNIMV-E 199
Cdd:COG0510     1 RLHAS-PALLRFD--LFARLERYL----------ALGPRDLPELL--RRLEELERALAaRPLPLVLCHGDLHPGNFLVtD 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1510996204 200 NGRFSgFIDCGRLGVADRYQDIALAtrdIAE-ELGGEWADRFLVLYGIAAPDS---QRIAFYRLLDEF 263
Cdd:COG0510    66 DGRLY-LIDWEYAGLGDPAFDLAAL---LVEyGLSPEQAEELLEAYGFGRPTEellRRLRAYRALADL 129
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
36-94 3.07e-04

Fructosamine-3-kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 41.34  E-value: 3.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  36 VFRLSAQGRPVlFVKTDLSGALNELQDEAARLSWLA-TTGVPCAAVLDVVTEAGRDWLLL 94
Cdd:COG3001    31 AYRVTTDGRRV-FVKLNPASPLGMFEAEAAGLRALAaTGTIRVPEVIGVGTTGDHAFLVL 89
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 73-223 2.53e-03

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 38.38  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510996204  73 TGVPcAAVLDVVTEAgRDWLLLGEVPGQDLLSShlapaekvsiMADAMRRLHTLDPATCPFDHQAKHRIERARTRMeagl 152
Cdd:cd05152    87 PGVP-AATIDPEIQN-YVWNWDPLAPPPVFARS----------LGKALAALHSIPADLAAAAGLPVYTAEEVRARM---- 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1510996204 153 vdQDDLDE-EHQGLAPAELFARLKARMPDG----EDLVVTHGDACLPNIMV-ENGRFSGFIDCGRLGVADRYQDIAL 223
Cdd:cd05152   151 --AARMDRvKETFGVPPALLARWQAWLADDslwpFHTVLVHGDLHPGHILVdEDGRVTGLIDWTEAKVGDPADDFAW 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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